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Institut de Biologie StructuraleGrenoble / France

Contact person(s) related to this article / THIELENS Nicole

Presentation of the "Immune response to pathogens and altered-self" group

Group leader: Nicole Thielens

The group shares a common interest for the molecular recognition mechanisms involved in various aspects of the immune response to pathogens and altered self cells, and for the biological implications of these interactions in anti-microbial defence, maintenance of immune tolerance and evasion strategies of pathogens.


Research topics

  • Innate immune proteins at the host-pathogen interface : structure and fonction
  • Altered self phagocytoseis : recognition and signalling
  • Antigen recognition in the cellular immune response

Key words

Apoptosis - Assembly - Complement - Innate immunity - Pathogens - Phagocytosis - Serine proteases - T cell receptor - Molecular recognition

Specialized techniques

Amino acid analysis - Cell culture - Kinetics of interactions (Biacore technology) - Protein engineering - Protein N-ter sequencing - X-ray crystallography

ISBG platforms steered by IRPAS group members

Amino acid analysis - Protein N-ter sequencing - Surface Plasmon Resonance (SPR) - Cellular Imaging

Most recent publications

- Wicker-Planquart, C., and J.-M. Jault. 2015. Interaction between Bacillus subtilis YsxC and ribosomes (or rRNAs). FEBS Lett. 589: 1026–1032.
- Awad, R., M. Sévajol, I. Ayala, A. Chouquet, P. Frachet, P. Gans, J.-B. Reiser, and J.-P. Kleman. 2015. The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif. FEBS Open Bio 5: 99–106.
- Sosoniuk, E., G. Vallejos, H. Kenawy, C. Gaboriaud, N. Thielens, T. Fujita, W. Schwaeble, A. Ferreira, and C. Valck. 2014. Trypanosoma cruzi calreticulin inhibits the complement lectin pathway activation by direct interaction with L-Ficolin. Mol. Immunol. 60: 80–85.
- Reiser, J.-B., F. Legoux, S. Gras, E. Trudel, A. Chouquet, A. Léger, M. L. Gorrec, P. Machillot, M. Bonneville, X. Saulquin, and D. Housset. 2014. Analysis of Relationships between Peptide/MHC Structural Features and Naive T Cell Frequency in Humans. J Immunol 193: 5816–5826.
- Gaboriaud, C., W. L. Ling, N. M. Thielens, I. Bally, and V. Rossi. 2014. Deciphering the fine details of c1 assembly and activation mechanisms: “mission impossible”? Front Immunol 5: 565.
- Laffly, E., M. Lacroix, L. Martin, E. Vassal-Stermann, N. M. Thielens, and C. Gaboriaud. 2014. Human ficolin-2 recognition versatility extended: an update on the binding of ficolin-2 to sulfated/phosphated carbohydrates. FEBS Lett. 588: 4694–4700.
- Vassal-Stermann, E., M. Lacroix, E. Gout, E. Laffly, C. M. Pedersen, L. Martin, A. Amoroso, R. R. Schmidt, U. Zähringer, C. Gaboriaud, A.-M. Di Guilmi, and N. M. Thielens. 2014. Human L-ficolin recognizes phosphocholine moieties of pneumococcal teichoic acid. J. Immunol. 193: 5699–5708.
- Rossi, V., I. Bally, M. Lacroix, G. J. Arlaud, and N. M. Thielens. 2014. Classical complement pathway components C1r and C1s: purification from human serum and in recombinant form and functional characterization. Methods Mol. Biol. 1100: 43–60.
- Verneret, M., P. Tacnet-Delorme, R. Osman, R. Awad, A. Grichine, J.-P. Kleman, and P. Frachet. 2014. Relative contribution of c1q and apoptotic cell-surface calreticulin to macrophage phagocytosis. J Innate Immun 6: 426–434.
- Bally, I., S. Ancelet, C. Moriscot, F. Gonnet, A. Mantovani, R. Daniel, G. Schoehn, G. J. Arlaud, and N. M. Thielens. 2013. Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sites. Proc. Natl. Acad. Sci. U.S.A. 110: 8650–8655.
- Gaboriaud, C., R. K. Gupta, L. Martin, M. Lacroix, L. Serre, F. Teillet, G. J. Arlaud, V. Rossi, and N. M. Thielens. 2013. The serine protease domain of MASP-3: enzymatic properties and crystal structure in complex with ecotin. PLoS ONE 8: e67962.
- Jacquet, M., M. Lacroix, S. Ancelet, E. Gout, C. Gaboriaud, N. M. Thielens, and V. Rossi. 2013. Deciphering complement receptor type 1 interactions with recognition proteins of the lectin complement pathway. J. Immunol. 190: 3721–3731.
- Foucher, A.-E., J.-B. Reiser, C. Ebel, D. Housset, and J.-M. Jault. 2012. Potassium Acts as a GTPase-Activating Element on Each Nucleotide-Binding Domain of the Essential Bacillus subtilis EngA. PLoS ONE 7: e46795.
- Sevajol, M., J. B. Reiser, A. Chouquet, J. Perard, I. Ayala, P. Gans, J. P. Kleman, and D. Housset. 2012. The C-terminal polyproline-containing region of ELMO contributes to an increase in the life-time of the ELMO-DOCK complex. Biochimie 94: 823–8.
- Terrasse, R., P. Tacnet-Delorme, C. Moriscot, J. Pérard, G. Schoehn, T. Vernet, N. M. Thielens, A. M. Di Guilmi, and P. Frachet. 2012. Human and pneumococcal cell surface glyceraldehyde-3-phosphate dehydrogenase (GAPDH) proteins are both ligands of human C1q protein. J. Biol. Chem. 287: 42620–42633.
- Gaboriaud, C., P. Frachet, N. M. Thielens, and G. J. Arlaud. 2011. The human c1q globular domain: structure and recognition of non-immune self ligands. Front Immunol 2: 92.

(The list of all the publications of the group is available here)